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Q86W56

- PARG_HUMAN

UniProt

Q86W56 - PARG_HUMAN

Protein

Poly(ADP-ribose) glycohydrolase

Gene

PARG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters.1 Publication

    Catalytic activityi

    Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei737 – 73711 Publication
    Binding sitei740 – 7401Substrate
    Binding sitei754 – 7541Substrate; via amide nitrogen
    Active sitei755 – 75511 Publication
    Active sitei756 – 75611 Publication
    Binding sitei795 – 7951SubstrateBy similarity

    GO - Molecular functioni

    1. poly(ADP-ribose) glycohydrolase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cellular response to DNA damage stimulus Source: Ensembl
    3. detection of bacterium Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(ADP-ribose) glycohydrolase (EC:3.2.1.143)
    Gene namesi
    Name:PARG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:8605. PARG.

    Subcellular locationi

    Isoform 1 : Nucleus 2 Publications
    Note: Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage.
    Isoform 2 : Cytoplasm 1 Publication
    Note: Translocates to the nucleus in response to DNA damage.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Ensembl
    3. mitochondrial matrix Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121K → A: Abolishes nuclear targeting; when associated with G-13. 1 Publication
    Mutagenesisi13 – 131R → G: Abolishes nuclear targeting; when associated with A-12. 1 Publication
    Mutagenesisi36 – 361R → A: No effect. 1 Publication
    Mutagenesisi37 – 371R → G: No effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA32940.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 976976Poly(ADP-ribose) glycohydrolasePRO_0000066602Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei133 – 1331Phosphoserine1 Publication
    Modified residuei137 – 1371Phosphoserine1 Publication
    Modified residuei197 – 1971Phosphoserine3 Publications
    Modified residuei199 – 1991Phosphothreonine3 Publications
    Modified residuei261 – 2611PhosphoserineBy similarity
    Modified residuei264 – 2641PhosphoserineBy similarity
    Modified residuei291 – 2911PhosphoserineBy similarity
    Modified residuei298 – 2981Phosphoserine1 Publication
    Modified residuei302 – 3021Phosphoserine1 Publication
    Modified residuei340 – 3401N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ86W56.
    PaxDbiQ86W56.
    PRIDEiQ86W56.

    PTM databases

    PhosphoSiteiQ86W56.

    Miscellaneous databases

    PMAP-CutDBQ86W56.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ86W56.
    BgeeiQ86W56.
    CleanExiHS_PARG.
    GenevestigatoriQ86W56.

    Organism-specific databases

    HPAiHPA021819.

    Interactioni

    Subunit structurei

    Interacts with PCNA.2 Publications

    Protein-protein interaction databases

    BioGridi114077. 3 interactions.
    IntActiQ86W56. 1 interaction.
    STRINGi9606.ENSP00000384408.

    Structurei

    Secondary structure

    1
    976
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi452 – 4565
    Helixi458 – 4603
    Turni464 – 4674
    Beta strandi480 – 4823
    Helixi486 – 4883
    Beta strandi497 – 5015
    Beta strandi520 – 5223
    Beta strandi532 – 5343
    Helixi535 – 5439
    Helixi550 – 55910
    Helixi562 – 5643
    Turni565 – 5673
    Helixi571 – 5799
    Helixi583 – 5919
    Helixi593 – 60210
    Helixi604 – 6074
    Beta strandi621 – 6266
    Helixi627 – 63812
    Turni652 – 6554
    Helixi662 – 6654
    Helixi672 – 68817
    Beta strandi694 – 7018
    Helixi708 – 7103
    Beta strandi718 – 7247
    Helixi726 – 7294
    Turni730 – 7323
    Beta strandi733 – 7397
    Turni743 – 7508
    Helixi754 – 7618
    Helixi763 – 7675
    Helixi768 – 7714
    Beta strandi779 – 7846
    Beta strandi790 – 7934
    Helixi796 – 7983
    Beta strandi800 – 8045
    Beta strandi815 – 8184
    Beta strandi820 – 8256
    Helixi832 – 8365
    Helixi838 – 85215
    Helixi859 – 8613
    Beta strandi865 – 8684
    Helixi873 – 8753
    Helixi879 – 89214
    Beta strandi897 – 9004
    Helixi905 – 92016
    Helixi925 – 93915
    Turni940 – 9423
    Beta strandi945 – 9473
    Helixi952 – 96110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A0DX-ray1.75A448-976[»]
    4B1GX-ray1.83A448-976[»]
    4B1HX-ray2.00A448-976[»]
    4B1IX-ray2.14A448-976[»]
    4B1JX-ray2.08A448-976[»]
    ProteinModelPortaliQ86W56.
    SMRiQ86W56. Positions 450-963.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 456456A-domainAdd
    BLAST
    Regioni610 – 795186CatalyticAdd
    BLAST
    Regioni726 – 7272Substrate binding
    Regioni869 – 8746Substrate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi10 – 167Nuclear localization signal1 Publication
    Motifi76 – 838PIP-box (PCNA interacting peptide)

    Domaini

    The PIP-box mediates interaction with PCNA and localization to replication foci.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG254589.
    HOVERGENiHBG053510.
    InParanoidiQ86W56.
    KOiK07759.
    PhylomeDBiQ86W56.
    TreeFamiTF323527.

    Family and domain databases

    InterProiIPR007724. Poly_GlycHdrlase.
    [Graphical view]
    PANTHERiPTHR12837. PTHR12837. 1 hit.
    PfamiPF05028. PARG_cat. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86W56-1) [UniParc]FASTAAdd to Basket

    Also known as: hPARG111

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV    50
    PPSSPACVPG RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE 100
    NNNTRIESMM SSVQKDNFYQ HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ 150
    TAAMCKWQNE GKHTEQLLES EPQTVTLVPE QFSNANIDRS PQNDDHSDTD 200
    SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS CDPGEDCASC 250
    QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP 300
    ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD 350
    IEFRKRYSTK GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS 400
    KQHGKKDSKI TDHFMRLPKA EDRRKEQWET KHQRTERKIP KYVPPHLSPD 450
    KKWLGTPIEE MRRMPRCGIR LPLLRPSANH TVTIRVDLLR AGEVPKPFPT 500
    HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ TALLNKFTRP 550
    QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI 600
    ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK 650
    SEYSSYPDIN FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ 700
    SLEDFPEWER CEKPLTRLHV TYEGTIEENG QGMLQVDFAN RFVGGGVTSA 750
    GLVQEEIRFL INPELIISRL FTEVLDHNEC LIITGTEQYS EYTGYAETYR 800
    WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK MRRELNKAYC 850
    GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF 900
    TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI 950
    KLYPFIYHAV ESCAETADHS GQRTGT 976
    Length:976
    Mass (Da):111,110
    Last modified:June 1, 2003 - v1
    Checksum:iD6646353C6D0180E
    GO
    Isoform 2 (identifier: Q86W56-2) [UniParc]FASTAAdd to Basket

    Also known as: hPARG102

    The sequence of this isoform differs from the canonical sequence as follows:
         1-82: Missing.

    Show »
    Length:894
    Mass (Da):102,312
    Checksum:i666B77E891E4A500
    GO
    Isoform 3 (identifier: Q86W56-3) [UniParc]FASTAAdd to Basket

    Also known as: hPARG99

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: Missing.

    Show »
    Length:868
    Mass (Da):99,432
    Checksum:i85BCE7201ABABA5F
    GO
    Isoform 4 (identifier: Q86W56-4) [UniParc]FASTAAdd to Basket

    Also known as: hPARG60

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MNAGPGCEPCTKRPR → MVQAGAEKDAQSISL
         16-423: Missing.
         485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W

    Note: Catalytically inactive.

    Show »
    Length:527
    Mass (Da):60,873
    Checksum:i0FBB26152C56D33D
    GO
    Isoform 5 (identifier: Q86W56-5) [UniParc]FASTAAdd to Basket

    Also known as: hPARG55

    The sequence of this isoform differs from the canonical sequence as follows:
         1-460: Missing.
         485-526: RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE → W

    Note: Catalytically inactive.

    Show »
    Length:475
    Mass (Da):54,794
    Checksum:i5443EFFA21AA84CE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 142RP → AT in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti61 – 611R → Q in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti127 – 1271E → V in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti138 – 1381P → L in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti227 – 2271Q → H in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti242 – 2421D → H in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti260 – 2601E → K in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti275 – 2751P → S in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti282 – 2821T → I in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti414 – 4141F → L in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti466 – 4661R → Q in AFM56043. (PubMed:22433848)Curated
    Sequence conflicti484 – 4841I → V in AFM56043. (PubMed:22433848)Curated
    Sequence conflicti814 – 8152WQ → CE in AAB61614. (PubMed:10449915)Curated
    Sequence conflicti817 – 8171R → H in AAH52966. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 460460Missing in isoform 5. 1 PublicationVSP_044674Add
    BLAST
    Alternative sequencei1 – 108108Missing in isoform 3. 2 PublicationsVSP_011770Add
    BLAST
    Alternative sequencei1 – 8282Missing in isoform 2. 2 PublicationsVSP_011769Add
    BLAST
    Alternative sequencei1 – 1515MNAGP…TKRPR → MVQAGAEKDAQSISL in isoform 4. 1 PublicationVSP_044675Add
    BLAST
    Alternative sequencei16 – 423408Missing in isoform 4. 1 PublicationVSP_044676Add
    BLAST
    Alternative sequencei485 – 52642RVDLL…PVEDE → W in isoform 4 and isoform 5. 2 PublicationsVSP_044677Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY258587 mRNA. Translation: AAP83314.1.
    AY575848 mRNA. Translation: AAT66421.1.
    AY575849 mRNA. Translation: AAT66422.1.
    AF005043 mRNA. Translation: AAB61614.1.
    EF382674 mRNA. Translation: ABR10027.1.
    JQ890226 mRNA. Translation: AFM56043.1.
    AK295786 mRNA. Translation: BAG58607.1.
    AK302560 mRNA. Translation: BAG63826.1.
    AK314909 mRNA. Translation: BAG37421.1.
    BC050560 mRNA. Translation: AAH50560.1.
    BC052966 mRNA. Translation: AAH52966.1.
    RefSeqiNP_003622.2. NM_003631.2. [Q86W56-1]
    UniGeneiHs.10136.
    Hs.535298.
    Hs.732225.

    Genome annotation databases

    EnsembliENST00000402038; ENSP00000384408; ENSG00000227345.
    GeneIDi8505.
    KEGGihsa:8505.
    UCSCiuc001jif.3. human. [Q86W56-1]
    uc010qgx.2. human. [Q86W56-3]

    Polymorphism databases

    DMDMi56417893.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY258587 mRNA. Translation: AAP83314.1 .
    AY575848 mRNA. Translation: AAT66421.1 .
    AY575849 mRNA. Translation: AAT66422.1 .
    AF005043 mRNA. Translation: AAB61614.1 .
    EF382674 mRNA. Translation: ABR10027.1 .
    JQ890226 mRNA. Translation: AFM56043.1 .
    AK295786 mRNA. Translation: BAG58607.1 .
    AK302560 mRNA. Translation: BAG63826.1 .
    AK314909 mRNA. Translation: BAG37421.1 .
    BC050560 mRNA. Translation: AAH50560.1 .
    BC052966 mRNA. Translation: AAH52966.1 .
    RefSeqi NP_003622.2. NM_003631.2. [Q86W56-1 ]
    UniGenei Hs.10136.
    Hs.535298.
    Hs.732225.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4A0D X-ray 1.75 A 448-976 [» ]
    4B1G X-ray 1.83 A 448-976 [» ]
    4B1H X-ray 2.00 A 448-976 [» ]
    4B1I X-ray 2.14 A 448-976 [» ]
    4B1J X-ray 2.08 A 448-976 [» ]
    ProteinModelPortali Q86W56.
    SMRi Q86W56. Positions 450-963.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114077. 3 interactions.
    IntActi Q86W56. 1 interaction.
    STRINGi 9606.ENSP00000384408.

    Chemistry

    BindingDBi Q86W56.
    ChEMBLi CHEMBL1795143.

    PTM databases

    PhosphoSitei Q86W56.

    Polymorphism databases

    DMDMi 56417893.

    Proteomic databases

    MaxQBi Q86W56.
    PaxDbi Q86W56.
    PRIDEi Q86W56.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000402038 ; ENSP00000384408 ; ENSG00000227345 .
    GeneIDi 8505.
    KEGGi hsa:8505.
    UCSCi uc001jif.3. human. [Q86W56-1 ]
    uc010qgx.2. human. [Q86W56-3 ]

    Organism-specific databases

    CTDi 8505.
    GeneCardsi GC10M051026.
    H-InvDB HIX0127080.
    HGNCi HGNC:8605. PARG.
    HPAi HPA021819.
    MIMi 603501. gene.
    neXtProti NX_Q86W56.
    PharmGKBi PA32940.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG254589.
    HOVERGENi HBG053510.
    InParanoidi Q86W56.
    KOi K07759.
    PhylomeDBi Q86W56.
    TreeFami TF323527.

    Miscellaneous databases

    ChiTaRSi PARG. human.
    GeneWikii PARG.
    GenomeRNAii 8505.
    NextBioi 31829.
    PMAP-CutDB Q86W56.
    PROi Q86W56.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86W56.
    Bgeei Q86W56.
    CleanExi HS_PARG.
    Genevestigatori Q86W56.

    Family and domain databases

    InterProi IPR007724. Poly_GlycHdrlase.
    [Graphical view ]
    PANTHERi PTHR12837. PTHR12837. 1 hit.
    Pfami PF05028. PARG_cat. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter sequence it shares with inner mitochondrial membrane translocase 23 (TIM23)."
      Meyer R.G., Meyer-Ficca M.L., Jacobson E.L., Jacobson M.K.
      Gene 314:181-190(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Skin.
    2. "Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments."
      Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L., Jacobson M.K.
      Exp. Cell Res. 297:521-532(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), MUTAGENESIS OF LYS-12; ARG-13; ARG-36 AND ARG-37, NUCLEAR LOCALIZATION SIGNAL.
      Tissue: Skin.
    3. "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization."
      Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.
      Cytogenet. Cell Genet. 85:269-270(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity."
      Meyer R.G., Meyer-Ficca M.L., Whatcott C.J., Jacobson E.L., Jacobson M.K.
      Exp. Cell Res. 313:2920-2936(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION.
      Tissue: Testis.
    5. "ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)."
      Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J., Moss J., Ziegler M.
      J. Biol. Chem. 287:16088-16102(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORMS 4 AND 5), ABSENCE OF CATALYTIC ACTIVITY (ISOFORMS 4 AND 5), SUBCELLULAR LOCATION.
      Tissue: Peripheral blood monocyte.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Brain cortex, Hippocampus and Testis.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Skin and Testis.
    8. "Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage."
      Haince J.F., Ouellet M.E., McDonald D., Hendzel M.J., Poirier G.G.
      Biochim. Biophys. Acta 1763:226-237(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197 AND THR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Proteomic investigation of phosphorylation sites in poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase."
      Gagne J.P., Moreel X., Gagne P., Labelle Y., Droit A., Chevalier-Pare M., Bourassa S., McDonald D., Hendzel M.J., Prigent C., Poirier G.G.
      J. Proteome Res. 8:1014-1029(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-197; THR-199 AND SER-298.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms."
      Mortusewicz O., Fouquerel E., Ame J.C., Leonhardt H., Schreiber V.
      Nucleic Acids Res. 39:5045-5056(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM 1), INTERACTION WITH PCNA.
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression."
      Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M., Schreiber V., Coin F.
      Mol. Cell 48:785-798(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives."
      Tucker J.A., Bennett N., Brassington C., Durant S.T., Hassall G., Holdgate G., McAlister M., Nissink J.W., Truman C., Watson M.
      PLoS ONE 7:E50889-E50889(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 448-976 ALONE AND IN COMPLEX WITH INHIBITORS, ACTIVE SITE, SUBSTRATE-BINDING SITES.

    Entry informationi

    Entry nameiPARG_HUMAN
    AccessioniPrimary (citable) accession number: Q86W56
    Secondary accession number(s): A5YBK3
    , B2RC24, B4DIU5, B4DYR4, I6RUV3, Q6E4P6, Q6E4P7, Q7Z742, Q9Y4W7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3